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Database: UniProt
Entry: B4CYS6_9BACT
LinkDB: B4CYS6_9BACT
Original site: B4CYS6_9BACT 
ID   B4CYS6_9BACT            Unreviewed;      1077 AA.
AC   B4CYS6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Membrane-bound dehydrogenase domain protein {ECO:0000313|EMBL:EDY20617.1};
GN   ORFNames=CfE428DRAFT_1814 {ECO:0000313|EMBL:EDY20617.1};
OS   Chthoniobacter flavus Ellin428.
OC   Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC   Chthoniobacteraceae; Chthoniobacter.
OX   NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY20617.1, ECO:0000313|Proteomes:UP000005824};
RN   [1] {ECO:0000313|EMBL:EDY20617.1, ECO:0000313|Proteomes:UP000005824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin428 {ECO:0000313|EMBL:EDY20617.1,
RC   ECO:0000313|Proteomes:UP000005824};
RX   PubMed=21460085; DOI=10.1128/JB.00295-11;
RA   Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA   Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA   Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA   Smidt H.;
RT   "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT   heterotrophic soil bacterium.";
RL   J. Bacteriol. 193:2902-2903(2011).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDY20617.1}.
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DR   EMBL; ABVL01000004; EDY20617.1; -; Genomic_DNA.
DR   RefSeq; WP_006979140.1; NZ_ABVL01000004.1.
DR   AlphaFoldDB; B4CYS6; -.
DR   STRING; 497964.CfE428DRAFT_1814; -.
DR   GeneID; 78184497; -.
DR   eggNOG; COG1413; Bacteria.
DR   eggNOG; COG2010; Bacteria.
DR   eggNOG; COG2133; Bacteria.
DR   eggNOG; COG3828; Bacteria.
DR   InParanoid; B4CYS6; -.
DR   Proteomes; UP000005824; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013428; Membrane-bound_put_N.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR   InterPro; IPR029010; ThuA-like.
DR   NCBIfam; TIGR02604; Piru_Ver_Nterm; 1.
DR   PANTHER; PTHR33546; LARGE, MULTIFUNCTIONAL SECRETED PROTEIN-RELATED; 1.
DR   PANTHER; PTHR33546:SF1; LARGE, MULTIFUNCTIONAL SECRETED PROTEIN-RELATED; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   Pfam; PF06283; ThuA; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000005824}.
FT   DOMAIN          986..1077
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   1077 AA;  118915 MW;  7C49779EAD80CEA5 CRC64;
     MINLRTLLLF FVLAISTYGA SGPIRVLFLG HEDLRVHNSC SAAALLMEKL GREAIYFDYV
     TTPDCLNRET LSHYDALMLY ANYPKISPDQ FAALNEFVES GHGFLPIHSA SACFGNEPRF
     IALVGARFKT HATGVFKAAI VDKAHPIMQG VNEYETWDET YIHDQHNTLG RKLLAERVEG
     AMREPWTWVR EQGKGRVFYT ASGHDKRTWE NADFQKMLRN AIIWSVGDTR RKDWERFLAQ
     REPEKREPNP YVANYEKRPE PITFQHPFSV KGSMDRTQVP ADMHLELFAA EPNIMKPIAL
     AWDDRGRCWV AETADYPHGV RPDGQGNDRI VICEDTDGDG RADKFTVFAD HLNLPTSLVF
     ANGGVIVSQA PKLLFLKSSK GDDHADVREV LMDGWGIRDT HAQANNLHYG LDNWIYGCVG
     YSGFKGTVGK KPLSFTQGTY RFKADGSTLE FLHQFSNNSW GQSFNAAGDD FGGTANNAPI
     FFGGIPATVV PEGMRVMTAK KINLEDKAHP ITTNYRQVDV FGGYTAATGS AFIYSSKLPP
     RMQGKAMVCE PTMKLISLMD VRPNGAGYVA KDAFNLVASS DEWMSPVFAE VGPDGAVWFV
     DWENFIVQHN PTPSVARGGF DAKTGAGGAH ENPLRDHSRG RIYRVVWDKA PQPAKITSLR
     GASTADLVKA LGSDTQQWRL TAQRLLVDGK KMDAVVALKR IVAANDGNIA AIHALWTLQG
     LQQLDDATVK AALSAKDSAL RRNAIRALSA DDRGYKSLIG TGVISDPDPA TRLAAMVKLG
     EMPTTPDIKN LVAKLAPEPI VQGDEWLKEA ARVLVQKHKV ITYKEGPNVL PNPGFEIVGT
     NGLPEGWKRR DNNKNEGTAS AEWRVVKDQP HSGGNAVRCF TRTEGDTSLF TDVPLKPNTR
     YRLSGWVKVH GFTGRASLND NGTQNETGRI TDKEGNWTEV ETFFDSGNRT TASINILHVG
     RGDTLYDDVK LCEVTADTGE EKLTAGDPKR GEQIFYKHQV ACVLCHSLRG QGSTVGPPLD
     GIARRATPAY IKESLLEPNK VLAKGYENLG TSPMPPMGLI LKPQELEDIQ AFLQTLR
//
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